TY - JOUR
T1 - Structural analysis and serological test of arginine periplasmic binding protein 2 from Chlamydophila pneumoniae
AU - Park, Sung Ha
AU - Chang, Ji Eun
AU - Hawkes, Hye Jin Kim
AU - Kang, Yeon Ho
AU - Hwang, Kwang Yeon
N1 - Funding Information:
We thank KJ Kim for his assistance in collecting the data at beamlines 4A and 6C of the Pohang Light Source, Korea. This work was supported by grants from the National R&D Program for the Functional Proteomics Center, 21C Frontier Program and in part by Global Frontier Program of a National Research Foundation of Korea (NRF) grant funded by the Korean Government.
PY - 2012/2/17
Y1 - 2012/2/17
N2 - The 'art' genes encode specific arginine uptake proteins, and are repressed by the repressible promoters of ArgR, affecting transcription of artJ [1,2]. Cpb0502, the arginine-binding periplasmic protein 2 precursor from Chlamydophila pneumoniae TW-183 strains, is responsible for arginine transport. As C. pneumoniae is difficult to isolate and culture, there have been many studies of better ways to detect it. A microimmunofluorescence assay (MIF) is still considered to be the 'gold standard' for detecting C. pneumoniae. Although MIF has its own limitations, a number of immunogenic antigens have been shown to be C. pneumoniae specific by this test. Here, we report Cpb0502 as a specific immunogenic antigen against C. pneumoniae as it was detected only in human infection sera of C. pneumoniae but not in Legionella pneumophila and Mycoplasma pneumoniae infection sera, showing high specificity and sensitivity by MIF, western blot and ELISA analysis. And also the crystal structure of Cpb0502 was determined to be a dimer at 2.07. å, revealing a similar backbone structure to a histidine kinase receptor, HK29S. Therefore we may suggest that Cpb0502 is a candidate immunogenic antigen for better diagnosis of C. pneumoniae.
AB - The 'art' genes encode specific arginine uptake proteins, and are repressed by the repressible promoters of ArgR, affecting transcription of artJ [1,2]. Cpb0502, the arginine-binding periplasmic protein 2 precursor from Chlamydophila pneumoniae TW-183 strains, is responsible for arginine transport. As C. pneumoniae is difficult to isolate and culture, there have been many studies of better ways to detect it. A microimmunofluorescence assay (MIF) is still considered to be the 'gold standard' for detecting C. pneumoniae. Although MIF has its own limitations, a number of immunogenic antigens have been shown to be C. pneumoniae specific by this test. Here, we report Cpb0502 as a specific immunogenic antigen against C. pneumoniae as it was detected only in human infection sera of C. pneumoniae but not in Legionella pneumophila and Mycoplasma pneumoniae infection sera, showing high specificity and sensitivity by MIF, western blot and ELISA analysis. And also the crystal structure of Cpb0502 was determined to be a dimer at 2.07. å, revealing a similar backbone structure to a histidine kinase receptor, HK29S. Therefore we may suggest that Cpb0502 is a candidate immunogenic antigen for better diagnosis of C. pneumoniae.
KW - Arginine periplasmic binding protein 2
KW - Chlamydophila pneumoniae
KW - Diagnosis
KW - Immunogenic antigen
KW - Serological test
KW - Structural analysis
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U2 - 10.1016/j.bbrc.2012.01.058
DO - 10.1016/j.bbrc.2012.01.058
M3 - Article
C2 - 22285188
AN - SCOPUS:84863150814
VL - 418
SP - 518
EP - 524
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -